摘要
β-1,3-葡聚糖酶广泛存在于细菌、真菌、植物和无脊椎动物中,因来源的差异,β-1,3葡聚糖酶的生理功能多样,如参与植物生长发育、提高或诱导抗病性、提供菌体营养、调节真菌细胞壁稳定性和刚性、参与病毒释放和入侵等。酶的结构研究是探索酶催化反应机理、挖掘酶催化特性以及酶理性设计改造的基础。本文对晶体结构研究最充分的GH16家族细菌β-1,3-葡聚糖酶的结构特征及催化机理进行综述,并通过与GH17家族植物来源β-1,3-葡聚糖酶的结构比较,揭示细菌β-1,3-葡聚糖酶的作用机制,为进一步改造和利用该酶,实现其在植物保护、食品和制药等领域的应用提供重要参考。
β-1,3-glucanases are widespread throughout bacteria,fungi,plants and invertebrates. They play various physiological roles due to the diversity of origin,such as participating in plant growth and development,defending against pathogens in plant,providing nutrients for bacteria,regulating fungal cell wall stability and rigidity,and involving in the release and invasion of virus.The research of enzyme structure is the basis to explore the mechanism of enzyme catalyzed reaction,to characterize enzyme catalytic properties and to design and transform the enzyme.The structure and catalytic mechanism of GH16 bacterial β-1,3-glucanase were thoroughly reviewed.By comparing with the structure of GH17 plant β-1,3-glucanases,this study was attempted to reveal how bacterial β-1,3-glucanases hydrolyze polysaccharide,and provides an important reference for further modification and utilization of bacterial β-1,3-glucanases in plant protection,food and pharmaceutical fields.
出处
《食品工业科技》
CAS
CSCD
北大核心
2017年第14期314-320,共7页
Science and Technology of Food Industry
基金
国家重点研发计划(2016YFD0200502)
辽宁省自然科学基金(2015020782)